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The DNA Polymerase Activity of Vaccinia Virus ‘Virosomes’: Solubilization and Properties

Fiona M. Tomley

Department of Bacteriology and Virology, Stopford Building, University of Manchester, Oxford Road, Manchester M13 9PT, U.K.

Intracellular DNA-protein complexes (‘virosomes’) of vaccinia virus have been isolated. The solubilization of the ‘virosome’-bound DNA polymerase activity was attempted by a variety of high-salt extraction procedures. The most efficient of these used 0.3 M-ammonium sulphate followed by brief sonication. The solubilized DNA polymerase activity from the ‘virosomes’, together with the DNA polymerases from 100000 g supernatant fluids from the cytoplasm of infected and uninfected cells were chromatographed on DEAE-cellulose and their properties compared. The ‘virosome’ DNA polymerase activity differed from the soluble vaccinia virus-induced DNA polymerase activity in its requirements for divalent cations and in respect of pH optimum, K_m for the deoxyribonucleoside triphosphates and the effect of N-ethylmaleimide.

Keywords: vaccinia virus, DNA ‘virosomes’, DNA polymerase

Present address: Department of Pathology, Division of Virology, Laboratories Block, Addenbrooke's Hospital, University of Cambridge, Hills Road, Cambridge CB2 2QQ, U.K.

Received 18 August 1983; accepted 29 December 1983.